Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Gustavo Fuertes
- Niccolo Banterle
- Kiersten M Ruff
- Aritra Chowdhury
- Rohit V Pappu
- Dmitri I Svergun
- Edward A Lemke
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000443547000004&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1126/science.aau8230
- eISSN
- 1095-9203
- Externe Identifier
- Clarivate Analytics Document Solution ID: GS3UB
- PubMed Identifier: 30166461
- ISSN
- 0036-8075
- Ausgabe der Veröffentlichung
- 6405
- Zeitschrift
- SCIENCE
- Artikelnummer
- ARTN aau8230
- Datum der Veröffentlichung
- 2018
- Status
- Published
- Titel
- Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"
- Sub types
- Editorial Material
- Ausgabe der Zeitschrift
- 361
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:p> Editors at <jats:italic>Science</jats:italic> requested our input on the above discussion (comment by Best <jats:italic>et al</jats:italic> . and response by Riback <jats:italic>et al</jats:italic> .) because both sets of authors use our data from Fuertes <jats:italic>et al</jats:italic> . (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods. </jats:p>
- Autoren
- Gustavo Fuertes
- Niccolo Banterle
- Kiersten M Ruff
- Aritra Chowdhury
- Rohit V Pappu
- Dmitri I Svergun
- Edward A Lemke
- DOI
- 10.1126/science.aau8230
- eISSN
- 1095-9203
- ISSN
- 0036-8075
- Ausgabe der Veröffentlichung
- 6405
- Zeitschrift
- Science
- Sprache
- en
- Datum der Veröffentlichung
- 2018
- Status
- Published
- Herausgeber
- American Association for the Advancement of Science (AAAS)
- Herausgeber URL
- http://dx.doi.org/10.1126/science.aau8230
- Datum der Datenerfassung
- 2024
- Titel
- Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”
- Ausgabe der Zeitschrift
- 361
Datenquelle: Crossref
- Abstract
- Editors at <i>Science</i> requested our input on the above discussion (comment by Best <i>et al</i> and response by Riback <i>et al</i>) because both sets of authors use our data from Fuertes <i>et al</i> (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods.
- Addresses
- European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
- Autoren
- Gustavo Fuertes
- Niccolo Banterle
- Kiersten M Ruff
- Aritra Chowdhury
- Rohit V Pappu
- Dmitri I Svergun
- Edward A Lemke
- DOI
- 10.1126/science.aau8230
- eISSN
- 1095-9203
- Externe Identifier
- PubMed Identifier: 30166461
- PubMed Central ID: PMC7611747
- Funding acknowledgements
- NINDS NIH HHS: R01 NS056114
- European Research Council: 646451
- European Research Council: 653706
- Open access
- false
- ISSN
- 0036-8075
- Ausgabe der Veröffentlichung
- 6405
- Zeitschrift
- Science (New York, N.Y.)
- Schlüsselwörter
- Water
- X-Ray Diffraction
- Protein Conformation
- Scattering, Small Angle
- Hydrophobic and Hydrophilic Interactions
- Intrinsically Disordered Proteins
- Sprache
- eng
- Medium
- Paginierung
- eaau8230
- Datum der Veröffentlichung
- 2018
- Status
- Published
- Datum der Datenerfassung
- 2018
- Titel
- Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".
- Sub types
- article-commentary
- Comment
- Research Support, N.I.H., Intramural
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 361
Files
https://science.sciencemag.org/content/sci/361/6405/eaau8230.full.pdf https://europepmc.org/articles/PMC7611747?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- Editors at Science requested our input on the above discussion (comment by Best et al and response by Riback et al) because both sets of authors use our data from Fuertes et al (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fluctuations that is intrinsic to finite-sized, heteropolymeric IDPs. Accounting for this decoupling resolves the discrepant inferences between the two methods, thus making a case for the utility of both methods.
- Date of acceptance
- 2018
- Autoren
- Gustavo Fuertes
- Niccolo Banterle
- Kiersten M Ruff
- Aritra Chowdhury
- Rohit V Pappu
- Dmitri I Svergun
- Edward A Lemke
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/30166461
- DOI
- 10.1126/science.aau8230
- eISSN
- 1095-9203
- Externe Identifier
- NIH Manuscript Submission ID: EMS134952
- PubMed Central ID: PMC7611747
- Funding acknowledgements
- European Research Council: 646451
- NINDS NIH HHS: R01 NS056114
- Ausgabe der Veröffentlichung
- 6405
- Zeitschrift
- Science
- Schlüsselwörter
- Hydrophobic and Hydrophilic Interactions
- Intrinsically Disordered Proteins
- Protein Conformation
- Scattering, Small Angle
- Water
- X-Ray Diffraction
- Sprache
- eng
- Country
- United States
- PII
- 361/6405/eaau8230
- Datum der Veröffentlichung
- 2018
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2018
- Titel
- Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water".
- Sub types
- Journal Article
- Research Support, N.I.H., Intramural
- Research Support, Non-U.S. Gov't
- Comment
- Ausgabe der Zeitschrift
- 361
Datenquelle: PubMed
- Beziehungen:
- Eigentum von